Direct interactions between molecular chaperones heat-shock protein (Hsp) 70 and Hsp40: Yeast Hsp70 Ssa1 binds the extreme C-terminal region of yeast Hsp40 Sis1

Biochemical Journal

Volumn 361, Issue 1, 2002, Pages 27-34

  Qian, Xinguo ^a   Hou, Wenbo ^a   Zhengang, Li ^a   Sha, Bingdong ^a  

^a UNIVERSITY OF ALABAMA AT BIRMINGHAM   (United States)

Author keywords

AFM; Atomic force microscopy; Isothermal titration calorimetry; ITC; Protein folding

Indexed keywords

ATOMIC FORCE MICROSCOPY; DEGRADATION; DIMERS; POLYPEPTIDES; YEAST;

CHAPERONES;

PROTEINS;

ADENOSINE TRIPHOSPHATASE; CHAPERONE; DIMER; FUNGAL PROTEIN; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; PROTIEN SIS1; UNCLASSIFIED DRUG;

ARTICLE; ATOMIC FORCE MICROSCOPY; CALORIMETRY; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONTROLLED STUDY; ENZYME ACTIVITY; IN VITRO STUDY; IONIC STRENGTH; NONHUMAN; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; TITRIMETRY; YEAST;

ADENOSINE TRIPHOSPHATASES; AMINO ACID SEQUENCE; CALORIMETRY; HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; MACROMOLECULAR SUBSTANCES; MICROSCOPY, ATOMIC FORCE; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN BINDING; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 0036177548     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3610027     Document Type: Article

References (22)

1. Protein folding in the cell
2. Heat shock proteins and molecular chaperones: Mediators of protein conformation and turnover in the cell
3. Molecular chaperones in cellular protein folding
4. The Hsp70 and Hsp60 chaperone machines
5. The emergence of the chaperone machines
6. Peptide-binding specificity of the molecular chaperone BiP
7. The role of Hsp70 in conferring unidirectionality on protein translocation into mitochondria
8. Polypeptide chain binding proteins: Catalysts of protein folding and related processes in cells
9. Structural analysis of substrate binding by the molecular chaperone DnaK
10. Three-dimensional structure of the ATPase fragment of a 70 K heat-shock cognate protein
11. The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1
12. Protein folding activity of Hsp70 is modified differentially by the Hsp40 cochaperones Sis1 and Ydj1
13. Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle
14. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
15. Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with Hdj-1
16. Characterization of SIS1, a S. cerevisiae homologue of bacteria dnaJ proteins
17. The yeast Sis1 protein, a DnaJ homolog, is required for the initiation of translation
18. The biochemical properties of the ATPase activity of a 70 kDa heat shock protein are governed by the C-terminal domains
19. Direct observation of enzyme activity with atomic force microscopy
20. Probing protein-protein interactions in real time
21. An essential role for the substrate-binding region of Hsp40s in Saccharomyces cerevisiae
22. Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons